Asparagine-linked sugar chains of plasma membrane glycoproteins from lymphoblastoid cells and acute lymphocytic leukemia cells

• Published in: Japanese Journal of Clinical Immunology Vol. 9; no. 4; pp. 249 - 255
• Main Authors: Orii, Tadao, Motoyosi, Fumiaki, Kondo, Naomi
• Format: Journal Article
• Language: English
• Published: The Japan Society for Clinical Immunology 1986
• Subjects: acute lymphocytic leukemia; asparagine-linked sugar chains of plasma membrane; B cell line; glycoproteins; oligosaccharide
• ISSN: 0911-4300; 1349-7413
• DOI: 10.2177/jsci.9.249

Asparagine-linked sugar chains of plasma membrane glycoproteins from acute lymphocytic leukemia cells (Null-ALL, Common ALL, Pre-B-ALL, T-ALL) and B lymphoblastoid cell lines (LCL) transformed by Epstein-Barr virus were investigated. The sugar chains were quantitatively liberated as radioactive oligosaccharides from polypeptide portion by hydrazinolysis followed by N-acetylation and NaB3H4 reduction. The structure of these sugar chains were determined by the chromatography and the sequential glycosidase digestion. In result, the main oligosaccharides in asparagine-linked sugar chains of plasma membrane glycoproteins in all type of the cells were biantennary complex sugar chains of Gal2•GlcNAc2•Man3•GlcNAc•Fuc•GlcNAcOT•Moreover, biantennary sugar chain with bisect N-acetylglu-cosamine (Gal2•GlcNAc2•Man3•GlcNAc•GlcNAc•Fuc•GlcNAcOT) was observed in only EAC+ Common ALL and LCL cells. Therefore it was suggested that this structure was concerned with the B cell function.